Results 21 to 30 of about 139,462,453 (100)

2-Keto-3-deoxy-6-phosphogalactonate Aldolase as a Catalyst for Stereocontrolled Carbon−Carbon Bond Formation

open access: yes, 2016
2-Keto-3-deoxy-6-phosphogalactonate Aldolase as a Catalyst for Stereocontrolled Carbon−Carbon Bond ...
Eric J. Toone (523230)   +3 more
core   +1 more source

Inititiating a structural study of 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli

open access: yes, 1999
2-Keto-3-deoxy-6-phosphogluconate aldolase (KDPG aldolase, E.C. 4.1.2.14) is a member of the pyruvate/phosphoenolpyruvate aldolase family. It is also a synthetically useful enzyme, capable of catalyzing the stereoselective aldol addition of pyruvate to a
Toone, EJ   +5 more
core   +2 more sources

Detection of aldolase activity on polyacrylamide gels: Application to 2-keto-4-hydroxyglutarate aldolase [PDF]

open access: yes, 1978
A method is described for the detection of 2-keto-4-hydroxyglutarate aldolase activity after electrophoresis of the enzyme on polyacrylamide gels. When gels are incubated with substrate (2-keto-4-hydroxyglutarate), activity is seen as a yellow-colored ...
Dekker, Eugene E., Lewinski, Neil D.
core   +1 more source

Constructing efficient bacterial cell factories to enable one‐carbon utilization based on quantitative biology: A review

open access: yesQuantitative Biology, Volume 12, Issue 1, Page 1-14, March 2024.
Abstract Developing methylotrophic cell factories that can efficiently catalyze organic one‐carbon (C1) feedstocks derived from electrocatalytic reduction of carbon dioxide into bio‐based chemicals and biofuels is of strategic significance for building a carbon‐neutral, sustainable economic and industrial system.
Yazhen Song   +9 more
wiley   +1 more source

The utilisation of gluconate by Escherichia coli K12.

open access: yes, 1974
Many micro-organisms catablise gluconate via the Entner-Doudoroff pathway. The key enzymes of this pathway are gluconate kinase, 6-phosphogluconate dehydratase (Edd) and 2-keto 5-deoxy 6-phosphogluconate (KDPG) aldolase.
Pelin. Faik (7702472)
core   +4 more sources

SYNTHESIS AND STRUCTURE PROOFS OF 2-KETO-3-DEOXY-OCTONIC ACIDS.

open access: yes, 1968
SYNTHESIS AND STRUCTURE PROOFS OF 2-KETO-3-DEOXY-OCTONIC ...
CHARLES LEE. HERSHBERGER (7994966)
core   +5 more sources

Gene expression and characterization of 2-keto-3-deoxy-gluconate kinase, a key enzyme in the modified Entner-Doudoroff pathway of Serratia marcescens KCTC 2172 [PDF]

open access: yes, 2009
We cloned 2-keto-3-deoxy-gluconate kinase (KDGK), which catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to 2-keto-3-deoxy-6-phophogluconate (KDPG) from Serratia marcescens KCTC 2172. The nucleotide sequence revealed a single open reading
Kim, H.-S.   +6 more
core   +4 more sources

Variant properties of bovine liver 2-keto-4-hydroxyglutarate aldolase; its [beta]-decarboxylase activity, lack of substrate stereospecificity, and structural requirements for binding substrate analogs [PDF]

open access: yes, 1971
1. 1. 2-Keto-4-hydroxyglutarate aldolase (2-oxo-4-hydroxyglutarate glyoxylatelyase; reaction: 2-oxo-4-hydroxyglutarate [left harpoon over right] pyruvate + glyoxylate) catalyzes the cleavage and the formation of both optical isomers of 2-keto-4 ...
Dekker, Eugene E., Kobes, Rodger D.
core   +1 more source

Characterization and crystal structure of Escherichia coli KDPGal aldolase

open access: yes, 2008
2-Keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) aldolases catalyze an identical reaction differing in substrate specificity in only the configuration of a single stereocenter.
Toone, Eric J.   +5 more
core   +1 more source

True and estimated flux values are compared for a subset of reactions of the E. coli central carbon metabolism network.

open access: yes, 2022
The difference is calculated between the true and estimated fluxes. Clearly, eiFlux accurately estimates the fluxes from a simulated set of measurements perturbed by simulated measurement error.
Daniel J. Lugar (12290519)   +1 more
core   +1 more source

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